We seek to understand the roles that protein and cofactor conformational and chemical dynamics play in biological energy transduction through the design and synthesis of peptides and small proteins. Towards this goal, we will elaborate new classes of de novo proteins that differ radically from natural photosynthetic systems and electron transfer proteins that will ultimately enable us to decipher the essential engineering criteria important for the efficient conversion of photonic energy into electrochemical potential energy. These investigations exploit de novo tetra-a-helical proteins engineered to bind donor-spacer-acceptor supermolecules and covalently linked multicofactor assemblies. We will strive to correlate structure, function, and dynamics in these systems, utilizing information derived from computational protein design, peptide synthesis, supermolecular chemistry, and ultrafast dynamical experiments that include transient optical pump / optical probe and visible pump / IR probe spectroscopies; this work will provide a deeper, more active understanding of (i) protein folding, (ii) how local electrostatic forces that surround donor, acceptor, and chromophore can be independently modulated, (iii) functional aspects of electron and proton coupled electron transfer and radical generation in proteins, and (iv) the essential dynamics of protein mediated energy transduction. [unreadable] [unreadable]